1VKN

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga maritima at 1.80 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
A	0005737	cellular_component	cytoplasm
A	0006526	biological_process	arginine biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A	0051287	molecular_function	NAD binding
A	0070401	molecular_function	NADP+ binding
B	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
B	0005737	cellular_component	cytoplasm
B	0006526	biological_process	arginine biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
B	0070401	molecular_function	NADP+ binding
C	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
C	0005737	cellular_component	cytoplasm
C	0006526	biological_process	arginine biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C	0051287	molecular_function	NAD binding
C	0070401	molecular_function	NADP+ binding
D	0003942	molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity
D	0005737	cellular_component	cytoplasm
D	0006526	biological_process	arginine biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D	0051287	molecular_function	NAD binding
D	0070401	molecular_function	NADP+ binding

Functional Information from PROSITE/UniProt

site_id	PS01224
Number of Residues	17
Details	ARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. VGnPGCYPTSvilALaP

Chain	Residue	Details
A	VAL140-PRO156

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00150

Chain	Residue	Details
A	CYS145
B	CYS145
C	CYS145
D	CYS145

---